...
首页> 外文期刊>Molecular cell >ATP Hydrolysis by the Proteasome Regulatory Complex PAN Serves Multiple Functions in Protein Degradation.
【24h】

ATP Hydrolysis by the Proteasome Regulatory Complex PAN Serves Multiple Functions in Protein Degradation.

机译:蛋白酶体调控复合物PAN的ATP水解在蛋白质降解中具有多种功能。

获取原文
获取原文并翻译 | 示例
           

摘要

To clarify the role of ATP in proteolysis, we studied archaeal 20S proteasomes and the PAN (proteasome-activating nucleotidase) regulatory complex, a homolog of the eukaryotic 19S ATPases. PAN's ATPase activity was stimulated similarly by globular (GFPssrA) and unfolded (casein) substrates, and by the ssrA recognition peptide. Denaturation of GFPssrA did not accelerate its degradation or eliminate the requirement for PAN and ATP. During degradation of one molecule of globular or unfolded substrates, 300-400 ATP molecules were hydrolyzed. An N-terminal deletion in the 20S alpha subunits caused opening of the substrate-entry channel and rapid degradation of unfolded proteins without PAN; however, degradation of globular GFPssrA still required PAN's ATPase activity, even after PAN-catalyzed unfolding. Thus, substrate binding activates ATP hydrolysis, which promotes three processes: substrate unfolding, gate opening in the 20S, and protein translocation.
机译:为了阐明ATP在蛋白水解中的作用,我们研究了古细菌20S蛋白酶体和PAN(蛋白酶体激活核苷酸酶)调控复合物,它是真核19S ATPase的同源物。球状(GFPssrA)和未折叠的(酪蛋白)底物,以及ssrA识别肽,都可以类似地刺激PAN的ATPase活性。 GFPssrA的变性不会加速其降解或消除对PAN和ATP的需求。在降解一分子球形或未折叠底物的过程中,水解了300-400个ATP分子。 20S alpha亚基的N末端缺失导致底物进入通道的打开和没有PAN的未折叠蛋白的快速降解;然而,即使在PAN催化的解折叠后,球状GFPssrA的降解仍需要PAN的ATPase活性。因此,底物结合激活了ATP水解,从而促进了三个过程:底物展开,20S中的门打开以及蛋白质易位。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号